5ZBB
Crystal structure of Rtt109-Asf1-H3-H4 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004402 | molecular_function | histone acetyltransferase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0006325 | biological_process | chromatin organization |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0006974 | biological_process | DNA damage response |
| A | 0010484 | molecular_function | histone H3 acetyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0032931 | molecular_function | histone H3K56 acetyltransferase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0006325 | biological_process | chromatin organization |
| C | 0000500 | cellular_component | RNA polymerase I upstream activating factor complex |
| C | 0000786 | cellular_component | nucleosome |
| C | 0003677 | molecular_function | DNA binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005694 | cellular_component | chromosome |
| C | 0006325 | biological_process | chromatin organization |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0006878 | biological_process | intracellular copper ion homeostasis |
| C | 0008823 | molecular_function | cupric reductase activity |
| C | 0009060 | biological_process | aerobic respiration |
| C | 0009303 | biological_process | rRNA transcription |
| C | 0030527 | molecular_function | structural constituent of chromatin |
| C | 0031298 | cellular_component | replication fork protection complex |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0042790 | biological_process | nucleolar large rRNA transcription by RNA polymerase I |
| C | 0043505 | cellular_component | CENP-A containing nucleosome |
| C | 0043935 | biological_process | sexual sporulation resulting in formation of a cellular spore |
| C | 0045943 | biological_process | positive regulation of transcription by RNA polymerase I |
| C | 0046982 | molecular_function | protein heterodimerization activity |
| C | 0070911 | biological_process | global genome nucleotide-excision repair |
| D | 0000500 | cellular_component | RNA polymerase I upstream activating factor complex |
| D | 0000786 | cellular_component | nucleosome |
| D | 0003677 | molecular_function | DNA binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005694 | cellular_component | chromosome |
| D | 0006325 | biological_process | chromatin organization |
| D | 0006334 | biological_process | nucleosome assembly |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0030527 | molecular_function | structural constituent of chromatin |
| D | 0031298 | cellular_component | replication fork protection complex |
| D | 0032991 | cellular_component | protein-containing complex |
| D | 0042790 | biological_process | nucleolar large rRNA transcription by RNA polymerase I |
| D | 0045943 | biological_process | positive regulation of transcription by RNA polymerase I |
| D | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 601 |
| Chain | Residue |
| A | TRP168 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 604 |
| Chain | Residue |
| A | LEU296 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 606 |
| Chain | Residue |
| A | GLN242 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 608 |
| Chain | Residue |
| A | SER109 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 609 |
| Chain | Residue |
| A | ARG464 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue IOD A 610 |
| Chain | Residue |
| A | ARG162 |
| A | GLU215 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue IOD A 611 |
| Chain | Residue |
| A | ARG170 |
| A | SER109 |
| A | ARG112 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue PEG A 612 |
| Chain | Residue |
| A | ALA93 |
| A | ASP94 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue IOD B 201 |
| Chain | Residue |
| B | VAL107 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue IOD C 201 |
| Chain | Residue |
| C | PHE84 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue IOD C 202 |
| Chain | Residue |
| C | LYS125 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue IOD C 204 |
| Chain | Residue |
| C | ARG63 |
| C | ARG63 |
| C | LYS64 |
| C | LYS64 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue IOD C 205 |
| Chain | Residue |
| C | SER86 |
| C | SER87 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue IOD C 208 |
| Chain | Residue |
| C | LYS121 |
| D | SER47 |
| D | LEU49 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue IOD D 201 |
| Chain | Residue |
| C | ARG63 |
| D | THR30 |
Functional Information from PROSITE/UniProt
| site_id | PS00047 |
| Number of Residues | 5 |
| Details | HISTONE_H4 Histone H4 signature. GAKRH |
| Chain | Residue | Details |
| D | GLY14-HIS18 |
| site_id | PS00322 |
| Number of Residues | 7 |
| Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
| Chain | Residue | Details |
| C | LYS14-LEU20 |
| site_id | PS00959 |
| Number of Residues | 9 |
| Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
| Chain | Residue | Details |
| C | PRO66-ILE74 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | DNA_BIND: |
| Chain | Residue | Details |
| D | LYS16-LYS20 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:22343720 |
| Chain | Residue | Details |
| D | LYS5 | |
| D | LYS8 | |
| D | LYS12 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:11080160, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592, ECO:0000269|PubMed:19113941 |
| Chain | Residue | Details |
| D | LYS16 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:22389435 |
| Chain | Residue | Details |
| D | LYS31 | |
| D | LYS77 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Omega-N-methylarginine => ECO:0000269|PubMed:19113941 |
| Chain | Residue | Details |
| D | ARG55 | |
| C | LYS56 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| D | SER60 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| D | SER64 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:16768447 |
| Chain | Residue | Details |
| D | LYS79 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-glutaryllysine => ECO:0000269|PubMed:31542297 |
| Chain | Residue | Details |
| D | LYS91 |
